Difference between revisions of "Part:BBa K1509001:Design"

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===References===
 
===References===
 
1.Busenlehner,  L.S., M.A. Pennella, and D.P. Giedroc, <em>The  SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural  insights into prokaryotic metal resistance.</em> FEMS Microbiol Rev, 2003. <strong>27</strong>(2-3): p. 131-43.
 
1.Busenlehner,  L.S., M.A. Pennella, and D.P. Giedroc, <em>The  SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural  insights into prokaryotic metal resistance.</em> FEMS Microbiol Rev, 2003. <strong>27</strong>(2-3): p. 131-43.
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2.Robinson,  N.J., S.K. Whitehall, and J.S. Cavet, <em>Microbial  metallothioneins.</em> Adv Microb Physiol, 2001. <strong>44</strong>: p. 183-213.
 
2.Robinson,  N.J., S.K. Whitehall, and J.S. Cavet, <em>Microbial  metallothioneins.</em> Adv Microb Physiol, 2001. <strong>44</strong>: p. 183-213.
  

Revision as of 13:15, 17 October 2014


A bi-directional promoter affected by SmtB protein


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

We got smt O-P and smtA, a fragment coding MT-like to sequester metal ions from smt locus by PCR and overlaped two fragments,smtB-smt O-P and pigment gene.Binding with smtB, smt O-P represses the expression of reporter genes.In the presence of heavy metal,the pigment and SmtA can expression normally.


Source

smt O-P is a part of smt locus from Synechococcus PCC7942.

References

1.Busenlehner, L.S., M.A. Pennella, and D.P. Giedroc, The SmtB/ArsR family of metalloregulatory transcriptional repressors: Structural insights into prokaryotic metal resistance. FEMS Microbiol Rev, 2003. 27(2-3): p. 131-43.

2.Robinson, N.J., S.K. Whitehall, and J.S. Cavet, Microbial metallothioneins. Adv Microb Physiol, 2001. 44: p. 183-213.

3.Erbe, J.L., K.B. Taylor, and L.M. Hall, Metalloregulation of the cyanobacterial smt locus: identification of SmtB binding sites and direct interaction with metals. Nucleic Acids Res, 1995. 23(13): p. 2472-8.

4.VanZile, M.L., X. Chen, and D.P. Giedroc, Allosteric negative regulation of smt O/P binding of the zinc sensor, SmtB, by metal ions: a coupled equilibrium analysis. Biochemistry, 2002. 41(31): p. 9776-86.

5.Morby, A.P., et al., SmtB is a metal-dependent repressor of the cyanobacterial metallothionein gene smtA: identification of a Zn inhibited DNA-protein complex. Nucleic Acids Res, 1993. 21(4): p. 921-5.

6.Huckle, J.W., et al., Isolation of a prokaryotic metallothionein locus and analysis of transcriptional control by trace metal ions. Mol Microbiol, 1993. 7(2): p. 177-87.

7.VanZile, M.L., X. Chen, and D.P. Giedroc, Structural characterization of distinct alpha3N and alpha5 metal sites in the cyanobacterial zinc sensor SmtB. Biochemistry, 2002. 41(31): p. 9765-75.

8.Kar, S.R., et al., The cyanobacterial repressor SmtB is predominantly a dimer and binds two Zn2+ ions per subunit. Biochemistry, 1997. 36(49): p. 15343-8.

9.Cook, W.J., et al., Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins. J Mol Biol, 1998. 275(2): p. 337-46.

10.Busenlehner, L.S., et al., Spectroscopic properties of the metalloregulatory Cd(II) and Pb(II) sites of S. aureus pI258 CadC. Biochemistry, 2001. 40(14): p. 4426-36.